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The endosomal sorting complex required for transport repairs the membrane to delay cell death

The endosomal sorting complex required for transport (ESCRT) machinery plays a key role in the repair of damaged plasma membranes with puncta form and removes pores from the plasma membrane in regulated cell death, apoptosis, necroptosis, pyroptosis, ferroptosis, and autophagy. ESCRT-I overexpressio...

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Autores principales: Yang, Ye, Wang, Min, Zhang, Ying-Ying, Zhao, Shu-Zhi, Gu, Song
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9622947/
https://www.ncbi.nlm.nih.gov/pubmed/36330465
http://dx.doi.org/10.3389/fonc.2022.1007446
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author Yang, Ye
Wang, Min
Zhang, Ying-Ying
Zhao, Shu-Zhi
Gu, Song
author_facet Yang, Ye
Wang, Min
Zhang, Ying-Ying
Zhao, Shu-Zhi
Gu, Song
author_sort Yang, Ye
collection PubMed
description The endosomal sorting complex required for transport (ESCRT) machinery plays a key role in the repair of damaged plasma membranes with puncta form and removes pores from the plasma membrane in regulated cell death, apoptosis, necroptosis, pyroptosis, ferroptosis, and autophagy. ESCRT-I overexpression and ESCRT-III-associated charged multivesicular body protein (CHMP) 4B participate in apoptosis, and the ESCRT-1 protein TSG 101 maintains low levels of ALIX and ALG-2 and prevents predisposition to apoptosis. The ESCRT-III components CHMP2A and CHMP4B are recruited to broken membrane bubble sites with the requirement of extracellular Ca(2+), remove membrane vesicles from cells, and delay the time required for active MLKL to mediate necroptosis, thus preserving cell survival. CHMP4B disturbed pyroptosis by recruiting around the plasma membrane neck to remove the GSDMD pores and preserve plasma membrane integrity depending on Ca(2+) influx. The accumulation of the ESCRT-III subunits CHMP5 and CHMP6 in the plasma membrane is increased by the classical ferroptosis activators erastin-1 and ras-selective lethal small molecule 3 (RSL3) upon cytosolic calcium influx and repairs the ferroptotic plasma membrane. ESCRT-III- and VPS4-induced macroautophagy, ESCRT-0-initiated microautophagy. ESCRT-I, ESCRT-II, ESCRT-III, ALIX, and VPS4A are recruited to damaged lysosomes and precede lysophagy, indicating that ESCRT is a potential target to overcome drug resistance during tumor therapy.
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spelling pubmed-96229472022-11-02 The endosomal sorting complex required for transport repairs the membrane to delay cell death Yang, Ye Wang, Min Zhang, Ying-Ying Zhao, Shu-Zhi Gu, Song Front Oncol Oncology The endosomal sorting complex required for transport (ESCRT) machinery plays a key role in the repair of damaged plasma membranes with puncta form and removes pores from the plasma membrane in regulated cell death, apoptosis, necroptosis, pyroptosis, ferroptosis, and autophagy. ESCRT-I overexpression and ESCRT-III-associated charged multivesicular body protein (CHMP) 4B participate in apoptosis, and the ESCRT-1 protein TSG 101 maintains low levels of ALIX and ALG-2 and prevents predisposition to apoptosis. The ESCRT-III components CHMP2A and CHMP4B are recruited to broken membrane bubble sites with the requirement of extracellular Ca(2+), remove membrane vesicles from cells, and delay the time required for active MLKL to mediate necroptosis, thus preserving cell survival. CHMP4B disturbed pyroptosis by recruiting around the plasma membrane neck to remove the GSDMD pores and preserve plasma membrane integrity depending on Ca(2+) influx. The accumulation of the ESCRT-III subunits CHMP5 and CHMP6 in the plasma membrane is increased by the classical ferroptosis activators erastin-1 and ras-selective lethal small molecule 3 (RSL3) upon cytosolic calcium influx and repairs the ferroptotic plasma membrane. ESCRT-III- and VPS4-induced macroautophagy, ESCRT-0-initiated microautophagy. ESCRT-I, ESCRT-II, ESCRT-III, ALIX, and VPS4A are recruited to damaged lysosomes and precede lysophagy, indicating that ESCRT is a potential target to overcome drug resistance during tumor therapy. Frontiers Media S.A. 2022-10-18 /pmc/articles/PMC9622947/ /pubmed/36330465 http://dx.doi.org/10.3389/fonc.2022.1007446 Text en Copyright © 2022 Yang, Wang, Zhang, Zhao and Gu https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Oncology
Yang, Ye
Wang, Min
Zhang, Ying-Ying
Zhao, Shu-Zhi
Gu, Song
The endosomal sorting complex required for transport repairs the membrane to delay cell death
title The endosomal sorting complex required for transport repairs the membrane to delay cell death
title_full The endosomal sorting complex required for transport repairs the membrane to delay cell death
title_fullStr The endosomal sorting complex required for transport repairs the membrane to delay cell death
title_full_unstemmed The endosomal sorting complex required for transport repairs the membrane to delay cell death
title_short The endosomal sorting complex required for transport repairs the membrane to delay cell death
title_sort endosomal sorting complex required for transport repairs the membrane to delay cell death
topic Oncology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9622947/
https://www.ncbi.nlm.nih.gov/pubmed/36330465
http://dx.doi.org/10.3389/fonc.2022.1007446
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